Nucleation of protein crystals
Nucleation of protein crystals
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DOI：
10.1016/s1047-8477(03)00035-2
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发表时间：
2003-04-01
影响因子：
3
通讯作者：
García-Ruiz, JM
中科院分区：
文献类型：
--
作者：
García-Ruiz, JM
本文介绍了成核理论在蛋白质溶液结晶中的应用。它表明，经典的方法解释了可用的成核数据在大多数条件下用于生长蛋白质晶体的结构研究和工业结晶。然而，它不能解释大多数关于临界团簇结构的实验数据。它还表明，开放系统的平衡工作，如悬滴和反扩散技术，奥斯特瓦尔德-迈尔斯蛋白质溶解度图的几何形状和形成晶体的数量，大小和质量不仅取决于过饱和度，但也对过饱和度的发展速度。(C)2003 Elsevier Science（美国）。All rights reserved.
This paper introduces nucleation theory applied to crystallizing protein solutions. It is shown that the classical approach explains the available nucleation data under most conditions used for growing protein crystals for structural studies and for industrial crystallization. However, it fails to explain most experimental data on the structure of the critical clusters. It is also shown that for open systems working out of equilibrium, such as hanging-drop and counterdiffusion techniques, the geometry of the Ostwald-Myers protein solubility diagram and the number, size, and quality of the forming crystals depend not only on supersaturation but also on the rate of development of supersaturation. (C) 2003 Elsevier Science (USA). All rights reserved.